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Politics often interferes where it has no natural business, and one of those places is the discussion among a teenager, her parents, and her doctor or between a woman and her doctor about the best choices for health. The hottest button politics is pushing right now takes the form of a tiny hormone-containing pill known popularly as the birth control pill or, simply, The Pill. This hormonal medication, when taken correctly (same time every day, every day), does indeed prevent pregnancy. But like just about any other medication, this one has multiple uses, the majority of them unrelated to pregnancy prevention.

But let’s start with pregnancy prevention first and get it out of the way. When I used to ask my students how these hormone pills work, they almost invariably answered, “By making your body think it is pregnant.” That’s not correct. We take advantage of our understanding of how our bodies regulate hormones not to mimic pregnancy, exactly, but instead to flatten out what we usually talk about as a hormone cycle.

The Menstrual Cycle

In a hormonally cycling girl or woman, the brain talks to the ovaries and the ovaries send messages to the uterus and back to the brain. All this chat takes place via chemicals called hormones. In human females, the ovarian hormones are progesterone and estradiol, a type of estrogen, and the brain hormones are luteinizing hormoneand follicle-stimulating hormone. The levels of these four hormones drive what we think of as the menstrual cycle, which exists to prepare an egg for fertilization and to make the uterine lining ready to receive a fertilized egg, should it arrive.

Fig. 1. Female reproductive anatomy. Credit: Jeanne Garbarino.

In the theoretical 28-day cycle, fertilization (fusion of sperm and egg), if it occurs, will happen about 14 days in, timed with ovulation, or release of the egg from the ovary into the Fallopian tube or oviduct (see video–watch for the tiny egg–and Figure 1). The fertilized egg will immediately start dividing, and a ball of cells (called a blastocyst) that ultimately develops is expected to arrive at the uterus a few days later.

If the ball of cells shows up and implants in the uterine wall, the ovary continues producing progesterone to keep that fluffy, welcoming uterine lining in place. If nothing shows up, the ovaries drop output of estradiol and progesterone so that the uterus releases its lining of cells (which girls and women recognize as their “period”), and the cycle starts all over again.

A typical cycle

The typical cycle (which almost no girl or woman seems to have) begins on day 1 when a girl or woman starts her “period.” This bleeding is the shedding of the uterine lining, a letting go of tissue because the ovaries have bottomed out production of the hormones that keep the tissue intact. During this time, the brain and ovaries are in communication. In the first two weeks of the cycle, called the “follicular phase” (see Figure 2), an ovary has the job of promoting an egg to mature. The egg is protected inside a follicle that spends about 14 days reaching maturity. During this time, the ovary produces estrogen at increasing levels, which causes thickening of the uterine lining, until the estradiol hits a peak about midway through the cycle. This spike sends a hormone signal to the brain, which responds with a hormone spike of its own.

Fig. 2. Top: Day of cycle and phases. Second row: Body temperature (at waking) through cycle.Third row: Hormones and their levels. Fourth row: What the ovaries are doing.Fifth row: What the uterus is doing. Via Wikimedia Commons.

In the figure, you can see this spike as the red line indicating luteinizing hormone. A smaller spike of follicle-stimulating hormone (blue line), also from the brain, occurs simultaneously. These two hormones along with the estradiol peak result in the follicle expelling the egg from the ovary into the Fallopian tube, or oviduct (Figure 3, step 4). That’s ovulation.

Fun fact: Right when the estrogen spikes, a woman’s body temperature will typically drop a bit (see “Basal body temperature” in the figure), so many women have used temperature monitoring to know that ovulation is happening. Some women also may experience a phenomenon called mittelschmerz, a pain sensation on the side where ovulation is occurring; ovaries trade off follicle duties with each cycle.

The window of time for a sperm to meet the egg is usually very short, about a day. Meanwhile, as the purple line in the “hormone level” section of Figure 2 shows, the ovary in question immediately begins pumping out progesterone, which maintains that proliferated uterine lining should a ball of dividing cells show up.

The structure in the ovary responsible for this phase, the luteal phase, is the corpus luteum (“yellow body”; see Figure 3, step 5), which puts out progesterone for a couple of weeks after ovulation to keep the uterine lining in place. If nothing implants, the corpus luteum degenerates (Figure 3, step 6). If implantation takes place, this structure will (should) instead continue producing progesterone through the early weeks of pregnancy to ensure that the lining doesn’t shed.

How do hormones in a pill stop all of this?

The hormones from the brain–luteinizing hormone and follicle-stimulating hormone– spike because the brain gets signals from the ovarian hormones. When a girl or woman takes the pills, which contain synthetics of ovarian hormones, the hormone dose doesn’t peak that way. Instead, the pills expose the girl or woman to a flat daily dose of hormones (synthetic estradiol and synthetic progesterone) or hormone (synthetic progesterone only). Without these peaks (and valleys), the brain doesn’t release the hormones that trigger follicle maturation or ovulation. Without follicle maturation and ovulation, no egg will be present for fertilization.

Most prescriptions of hormone pills are for packets of 28 pills. Typically, seven of these pills–sometimes fewer–are “dummy pills.” During the time a woman takes these dummy pills, her body shows the signs of withdrawal from the hormones, usually as a fairly light bleeding for those days, known as “withdrawal bleeding.” With the lowest-dose pills, the uterine lining may proliferate very little, so that this bleeding can be quite light compared to what a woman might experience under natural hormone influences.

How important are hormonal interventions for birth control?

Every woman has a story to tell, and the stories about the importance of hormonal birth control are legion. My personal story is this: I have three children. With our last son, I had two transient ischemic attacks at the end of the pregnancy, tiny strokes resulting from high blood pressure in the pregnancy. I had to undergo an immediate induction. This was the second time I’d had this condition, called pre-eclampsia, having also had this with our first son. My OB-GYN told me under no uncertain terms that I could not–should not–get pregnant again, as a pregnancy could be life threatening.

But I’m married, happily. As my sister puts it, my husband and I “like each other.” We had to have a failsafe method of ensuring that I wouldn’t become pregnant and endanger my life. For several years, hormonal medication made that possible. After I began having cluster headaches and high blood pressure on this medication in my forties, my OB-GYN and I talked about options, and we ultimately turned to surgery to prevent pregnancy.

But surgery is almost always not reversible. For a younger woman, it’s not the temporary option that hormonal pills provide. Hormonal interventions also are available in other forms, including as a vaginal ring, intrauterine device (some are hormonal), and implants, all reversible.

One of the most important things a society can do for its own health is to ensure that women in that society have as much control as possible over their reproduction. Thanks to hormonal interventions, although I’ve been capable of childbearing for 30 years, I’ve had only three children in that time. The ability to control my childbearing has meant I’ve been able to focus on being the best woman, mother, friend, and partner I can be, not only for myself and my family, but as a contributor to society, as well.

What are other uses of hormonal interventions?

Heavy, painful, or irregular periods. Did you read that part about how flat hormone inputs can mean less build up of the uterine lining and thus less bleeding and a shorter period? Many girls and women who lack hormonal interventions experience bleeding so heavy that they become anemic. This kind of bleeding can take a girl or woman out of commission for days at a time, in addition to threatening her health. Pain and irregular bleeding also are disabling and negatively affect quality of life on a frequent basis. Taking a single pill each day can make it all better.

Unfortunately, the current political climate can take this situation–especially for teenage girls–and cast it as a personal moral failing with implications that a girl who takes hormonal medications is a “slut,” rather than the real fact that this hormonal intervention is literally maintaining the regularity of her health.

For some context, imagine that a whenever a boy or man produced sperm, it was painful or caused extensive blood loss that resulted in anemia. Would there be any issues raised with providing a medication that successfully addressed this problem?

Polycystic ovarian syndrome. This syndrome is, at its core, an imbalance of the ovarian hormones that is associated with all kinds of problems, from acne to infertility to overweight touterine cancer. Guess what balances those hormones back out? Yes. Hormonal medication, otherwise known as The Pill.

Again, for some context, imagine that this syndrome affected testes instead of ovaries, and caused boys and men to become infertile, experience extreme pain in the testes, gain weight, be at risk for diabetes, and lose their hair. Would there be an issue with providing appropriate hormonal medication to address this problem?

Acne. I had a friend in high school who was on hormonal medication, not because she was sexually active (she was not) but because she struggled for years with acne. This is an FDA-approved use of this medication.

Are there health benefits of hormonal interventions?

In a word, yes. They can protect against certain cancers, including ovarian and endometrial, or uterine, cancer. Women die from these cancers, and this protection is not negligible. They may also help protect against osteoporosis, or bone loss. In cases like mine, they protect against a potentially life-threatening pregnancy.

Yes. No medical intervention is without risk. In the case of hormonal interventions, lifestyle habits such as smoking can enhance risk for high blood pressure and blood clots. Age can be a factor, although–as I can attest–women no longer have to stop taking hormonal interventions after age 35 as long as they are nonsmokers and blood pressure is normal. These interventions have been associated with a decrease in some cancers, as I’ve noted, but also with an increase in others, such as liver cancer, over the long term. The effect on breast cancer risk is mixed and may have to do with how long taking the medication delays childbearing. ETA: PLoS Medicine just published a paper (open access) addressing the effects of hormonal interventions on cancer risk.

The four basic categories of molecules for building life are carbohydrates, lipids, proteins, and nucleic acids.

Carbohydrates serve many purposes, from energy to structure to chemical communication, as monomers or polymers.

Lipids, which are hydrophobic, also have different purposes, including energy storage, structure, and signaling.

Proteins, made of amino acids in up to four structural levels, are involved in just about every process of life.

The nucleic acids DNA and RNA consist of four nucleotide building blocks, and each has different purposes.

The longer version

Life is so diverse and unwieldy, it may surprise you to learn that we can break it down into four basic categories of molecules. Possibly even more implausible is the fact that two of these categories of large molecules themselves break down into a surprisingly small number of building blocks. The proteins that make up all of the living things on this planet and ensure their appropriate structure and smooth function consist of only 20 different kinds of building blocks. Nucleic acids, specifically DNA, are even more basic: only four different kinds of molecules provide the materials to build the countless different genetic codes that translate into all the different walking, swimming, crawling, oozing, and/or photosynthesizing organisms that populate the third rock from the Sun.

Big Molecules with Small Building Blocks

The functional groups, assembled into building blocks on backbones of carbon atoms, can be bonded together to yield large molecules that we classify into four basic categories. These molecules, in many different permutations, are the basis for the diversity that we see among living things. They can consist of thousands of atoms, but only a handful of different kinds of atoms form them. It’s like building apartment buildings using a small selection of different materials: bricks, mortar, iron, glass, and wood. Arranged in different ways, these few materials can yield a huge variety of structures.

We encountered functional groups and the SPHONC in Chapter 3. These components form the four categories of molecules of life. These Big Four biological molecules are carbohydrates, lipids, proteins, and nucleic acids. They can have many roles, from giving an organism structure to being involved in one of the millions of processes of living. Let’s meet each category individually and discover the basic roles of each in the structure and function of life.

Carbohydrates

You have met carbohydrates before, whether you know it or not. We refer to them casually as “sugars,” molecules made of carbon, hydrogen, and oxygen. A sugar molecule has a carbon backbone, usually five or six carbons in the ones we’ll discuss here, but it can be as few as three. Sugar molecules can link together in pairs or in chains or branching “trees,” either for structure or energy storage.

When you look on a nutrition label, you’ll see reference to “sugars.” That term includes carbohydrates that provide energy, which we get from breaking the chemical bonds in a sugar called glucose. The “sugars” on a nutrition label also include those that give structure to a plant, which we call fiber. Both are important nutrients for people.

Sugars serve many purposes. They give crunch to the cell walls of a plant or the exoskeleton of a beetle and chemical energy to the marathon runner. When attached to other molecules, like proteins or fats, they aid in communication between cells. But before we get any further into their uses, let’s talk structure.

The sugars we encounter most in basic biology have their five or six carbons linked together in a ring. There’s no need to dive deep into organic chemistry, but there are a couple of essential things to know to interpret the standard representations of these molecules.

Check out the sugars depicted in the figure. The top-left molecule, glucose, has six carbons, which have been numbered. The sugar to its right is the same glucose, with all but one “C” removed. The other five carbons are still there but are inferred using the conventions of organic chemistry: Anywhere there is a corner, there’s a carbon unless otherwise indicated. It might be a good exercise for you to add in a “C” over each corner so that you gain a good understanding of this convention. You should end up adding in five carbon symbols; the sixth is already given because that is conventionally included when it occurs outside of the ring.

On the left is a glucose with all of its carbons indicated. They’re also numbered, which is important to understand now for information that comes later. On the right is the same molecule, glucose, without the carbons indicated (except for the sixth one). Wherever there is a corner, there is a carbon, unless otherwise indicated (as with the oxygen). On the bottom left is ribose, the sugar found in RNA. The sugar on the bottom right is deoxyribose. Note that at carbon 2 (*), the ribose and deoxyribose differ by a single oxygen.

The lower left sugar in the figure is a ribose. In this depiction, the carbons, except the one outside of the ring, have not been drawn in, and they are not numbered. This is the standard way sugars are presented in texts. Can you tell how many carbons there are in this sugar? Count the corners and don’t forget the one that’s already indicated!

If you said “five,” you are right. Ribose is a pentose (pent = five) and happens to be the sugar present in ribonucleic acid, or RNA. Think to yourself what the sugar might be in deoxyribonucleic acid, or DNA. If you thought, deoxyribose, you’d be right.

The fourth sugar given in the figure is a deoxyribose. In organic chemistry, it’s not enough to know that corners indicate carbons. Each carbon also has a specific number, which becomes important in discussions of nucleic acids. Luckily, we get to keep our carbon counting pretty simple in basic biology. To count carbons, you start with the carbon to the right of the non-carbon corner of the molecule. The deoxyribose or ribose always looks to me like a little cupcake with a cherry on top. The “cherry” is an oxygen. To the right of that oxygen, we start counting carbons, so that corner to the right of the “cherry” is the first carbon. Now, keep counting. Here’s a little test: What is hanging down from carbon 2 of the deoxyribose?

If you said a hydrogen (H), you are right! Now, compare the deoxyribose to the ribose. Do you see the difference in what hangs off of the carbon 2 of each sugar? You’ll see that the carbon 2 of ribose has an –OH, rather than an H. The reason the deoxyribose is called that is because the O on the second carbon of the ribose has been removed, leaving a “deoxyed” ribose. This tiny distinction between the sugars used in DNA and RNA is significant enough in biology that we use it to distinguish the two nucleic acids.

In fact, these subtle differences in sugars mean big differences for many biological molecules. Below, you’ll find a couple of ways that apparently small changes in a sugar molecule can mean big changes in what it does. These little changes make the difference between a delicious sugar cookie and the crunchy exoskeleton of a dung beetle.

Sugar and Fuel

A marathon runner keeps fuel on hand in the form of “carbs,” or sugars. These fuels provide the marathoner’s straining body with the energy it needs to keep the muscles pumping. When we take in sugar like this, it often comes in the form of glucose molecules attached together in a polymer called starch. We are especially equipped to start breaking off individual glucose molecules the minute we start chewing on a starch.

Double X Extra: A monomer is a building block (mono = one) and a polymer is a chain of monomers. With a few dozen monomers or building blocks, we get millions of different polymers. That may sound nutty until you think of the infinity of values that can be built using only the numbers 0 through 9 as building blocks or the intricate programming that is done using only a binary code of zeros and ones in different combinations.

Our bodies then can rapidly take the single molecules, or monomers, into cells and crack open the chemical bonds to transform the energy for use. The bonds of a sugar are packed with chemical energy that we capture to build a different kind of energy-containing molecule that our muscles access easily. Most species rely on this process of capturing energy from sugars and transforming it for specific purposes.

Polysaccharides: Fuel and Form

Plants use the Sun’s energy to make their own glucose, and starch is actually a plant’s way of storing up that sugar. Potatoes, for example, are quite good at packing away tons of glucose molecules and are known to dieticians as a “starchy” vegetable. The glucose molecules in starch are packed fairly closely together. A string of sugar molecules bonded together through dehydration synthesis, as they are in starch, is a polymer called a polysaccharide (poly = many; saccharide = sugar). When the monomers of the polysaccharide are released, as when our bodies break them up, the reaction that releases them is called hydrolysis.

Double X Extra: The specific reaction that hooks one monomer to another in a covalent bond is called dehydration synthesis because in making the bond–synthesizing the larger molecule–a molecule of water is removed (dehydration). The reverse is hydrolysis (hydro = water; lysis = breaking), which breaks the covalent bond by the addition of a molecule of water.

Although plants make their own glucose and animals acquire it by eating the plants, animals can also package away the glucose they eat for later use. Animals, including humans, store glucose in a polysaccharide called glycogen, which is more branched than starch. In us, we build this energy reserve primarily in the liver and access it when our glucose levels drop.

Whether starch or glycogen, the glucose molecules that are stored are bonded together so that all of the molecules are oriented the same way. If you view the sixth carbon of the glucose to be a “carbon flag,” you’ll see in the figure that all of the glucose molecules in starch are oriented with their carbon flags on the upper left.

The orientation of monomers of glucose in polysaccharides can make a big difference in the use of the polymer. The glucoses in the molecule on the top are all oriented “up” and form starch. The glucoses in the molecule on the bottom alternate orientation to form cellulose, which is quite different in its function from starch.

Storing up sugars for fuel and using them as fuel isn’t the end of the uses of sugar. In fact, sugars serve as structural molecules in a huge variety of organisms, including fungi, bacteria, plants, and insects.

The primary structural role of a sugar is as a component of the cell wall, giving the organism support against gravity. In plants, the familiar old glucose molecule serves as one building block of the plant cell wall, but with a catch: The molecules are oriented in an alternating up-down fashion. The resulting structural sugar is called cellulose.

That simple difference in orientation means the difference between a polysaccharide as fuel for us and a polysaccharide as structure. Insects take it step further with the polysaccharide that makes up their exoskeleton, or outer shell. Once again, the building block is glucose, arranged as it is in cellulose, in an alternating conformation. But in insects, each glucose has a little extra added on, a chemical group called an N-acetyl group. This addition of a single functional group alters the use of cellulose and turns it into a structural molecule that gives bugs that special crunchy sound when you accidentally…ahem…step on them.

These variations on the simple theme of a basic carbon-ring-as-building-block occur again and again in biological systems. In addition to serving roles in structure and as fuel, sugars also play a role in function. The attachment of subtly different sugar molecules to a protein or a lipid is one way cells communicate chemically with one another in refined, regulated interactions. It’s as though the cells talk with each other using a specialized, sugar-based vocabulary. Typically, cells display these sugary messages to the outside world, making them available to other cells that can recognize the molecular language.

Lipids: The Fatty Trifecta

Starch makes for good, accessible fuel, something that we immediately attack chemically and break up for quick energy. But fats are energy that we are supposed to bank away for a good long time and break out in times of deprivation. Like sugars, fats serve several purposes, including as a dense source of energy and as a universal structural component of cell membranes everywhere.

Fats: the Good, the Bad, the Neutral

Turn again to a nutrition label, and you’ll see a few references to fats, also known as lipids. (Fats are slightly less confusing that sugars in that they have only two names.) The label may break down fats into categories, including trans fats, saturated fats, unsaturated fats, and cholesterol. You may have learned that trans fats are “bad” and that there is good cholesterol and bad cholesterol, but what does it all mean?

Let’s start with what we mean when we say saturated fat. The question is, saturated with what? There is a specific kind of dietary fat call the triglyceride. As its name implies, it has a structural motif in which something is repeated three times. That something is a chain of carbons and hydrogens, hanging off in triplicate from a head made of glycerol, as the figure shows. Those three carbon-hydrogen chains, or fatty acids, are the “tri” in a triglyceride. Chains like this can be many carbons long.

Double X Extra: We call a fatty acid a fatty acid because it’s got a carboxylic acid attached to a fatty tail. A triglyceride consists of three of these fatty acids attached to a molecule called glycerol. Our dietary fat primarily consists of these triglycerides.

Triglycerides come in several forms. You may recall that carbon can form several different kinds of bonds, including single bonds, as with hydrogen, and double bonds, as with itself. A chain of carbon and hydrogens can have every single available carbon bond taken by a hydrogen in single covalent bond. This scenario of hydrogen saturation yields a saturated fat. The fat is saturated to its fullest with every covalent bond taken by hydrogens single bonded to the carbons.

Saturated fats have predictable characteristics. They lie flat easily and stick to each other, meaning that at room temperature, they form a dense solid. You will realize this if you find a little bit of fat on you to pinch. Does it feel pretty solid? That’s because animal fat is saturated fat. The fat on a steak is also solid at room temperature, and in fact, it takes a pretty high heat to loosen it up enough to become liquid. Animals are not the only organisms that produce saturated fat–avocados and coconuts also are known for their saturated fat content.

The top graphic above depicts a triglyceride with the glycerol, acid, and three hydrocarbon tails. The tails of this saturated fat, with every possible hydrogen space occupied, lie comparatively flat on one another, and this kind of fat is solid at room temperature. The fat on the bottom, however, is unsaturated, with bends or kinks wherever two carbons have double bonded, booting a couple of hydrogens and making this fat unsaturated, or lacking some hydrogens. Because of the space between the bumps, this fat is probably not solid at room temperature, but liquid.

You can probably now guess what an unsaturated fat is–one that has one or more hydrogens missing. Instead of single bonding with hydrogens at every available space, two or more carbons in an unsaturated fat chain will form a double bond with carbon, leaving no space for a hydrogen. Because some carbons in the chain share two pairs of electrons, they physically draw closer to one another than they do in a single bond. This tighter bonding result in a “kink” in the fatty acid chain.

In a fat with these kinks, the three fatty acids don’t lie as densely packed with each other as they do in a saturated fat. The kinks leave spaces between them. Thus, unsaturated fats are less dense than saturated fats and often will be liquid at room temperature. A good example of a liquid unsaturated fat at room temperature is canola oil.

A few decades ago, food scientists discovered that unsaturated fats could be resaturated or hydrogenated to behave more like saturated fats and have a longer shelf life. The process of hydrogenation–adding in hydrogens–yields trans fat. This kind of processed fat is now frowned upon and is being removed from many foods because of its associations with adverse health effects. If you check a food label and it lists among the ingredients “partially hydrogenated” oils, that can mean that the food contains trans fat.

Double X Extra: A triglyceride can have up to three different fatty acids attached to it. Canola oil, for example, consists primarily of oleic acid, linoleic acid, and linolenic acid, all of which are unsaturated fatty acids with 18 carbons in their chains.

Why do we take in fat anyway? Fat is a necessary nutrient for everything from our nervous systems to our circulatory health. It also, under appropriate conditions, is an excellent way to store up densely packaged energy for the times when stores are running low. We really can’t live very well without it.

Phospholipids: An Abundant Fat

You may have heard that oil and water don’t mix, and indeed, it is something you can observe for yourself. Drop a pat of butter–pure saturated fat–into a bowl of water and watch it just sit there. Even if you try mixing it with a spoon, it will just sit there. Now, drop a spoon of salt into the water and stir it a bit. The salt seems to vanish. You’ve just illustrated the difference between a water-fearing (hydrophobic) and a water-loving (hydrophilic) substance.

Generally speaking, compounds that have an unequal sharing of electrons (like ions or anything with a covalent bond between oxygen and hydrogen or nitrogen and hydrogen) will be hydrophilic. The reason is that a charge or an unequal electron sharing gives the molecule polarity that allows it to interact with water through hydrogen bonds. A fat, however, consists largely of hydrogen and carbon in those long chains. Carbon and hydrogen have roughly equivalent electronegativities, and their electron-sharing relationship is relatively nonpolar. Fat, lacking in polarity, doesn’t interact with water. As the butter demonstrated, it just sits there.

There is one exception to that little maxim about fat and water, and that exception is the phospholipid. This lipid has a special structure that makes it just right for the job it does: forming the membranes of cells. A phospholipid consists of a polar phosphate head–P and O don’t share equally–and a couple of nonpolar hydrocarbon tails, as the figure shows. If you look at the figure, you’ll see that one of the two tails has a little kick in it, thanks to a double bond between the two carbons there.

Phospholipids form a double layer and are the major structural components of cell membranes. Their bend, or kick, in one of the hydrocarbon tails helps ensure fluidity of the cell membrane. The molecules are bipolar, with hydrophilic heads for interacting with the internal and external watery environments of the cell and hydrophobic tails that help cell membranes behave as general security guards.

The kick and the bipolar (hydrophobic and hydrophilic) nature of the phospholipid make it the perfect molecule for building a cell membrane. A cell needs a watery outside to survive. It also needs a watery inside to survive. Thus, it must face the inside and outside worlds with something that interacts well with water. But it also must protect itself against unwanted intruders, providing a barrier that keeps unwanted things out and keeps necessary molecules in.

Phospholipids achieve it all. They assemble into a double layer around a cell but orient to allow interaction with the watery external and internal environments. On the layer facing the inside of the cell, the phospholipids orient their polar, hydrophilic heads to the watery inner environment and their tails away from it. On the layer to the outside of the cell, they do the same.

As the figure shows, the result is a double layer of phospholipids with each layer facing a polar, hydrophilic head to the watery environments. The tails of each layer face one another. They form a hydrophobic, fatty moat around a cell that serves as a general gatekeeper, much in the way that your skin does for you. Charged particles cannot simply slip across this fatty moat because they can’t interact with it. And to keep the fat fluid, one tail of each phospholipid has that little kick, giving the cell membrane a fluid, liquidy flow and keeping it from being solid and unforgiving at temperatures in which cells thrive.

Steroids: Here to Pump You Up?

Our final molecule in the lipid fatty trifecta is cholesterol. As you may have heard, there are a few different kinds of cholesterol, some of which we consider to be “good” and some of which is “bad.” The good cholesterol, high-density lipoprotein, or HDL, in part helps us out because it removes the bad cholesterol, low-density lipoprotein or LDL, from our blood. The presence of LDL is associated with inflammation of the lining of the blood vessels, which can lead to a variety of health problems.

But cholesterol has some other reasons for existing. One of its roles is in the maintenance of cell membrane fluidity. Cholesterol is inserted throughout the lipid bilayer and serves as a block to the fatty tails that might otherwise stick together and become a bit too solid.

Cholesterol’s other starring role as a lipid is as the starting molecule for a class of hormones we called steroids or steroid hormones. With a few snips here and additions there, cholesterol can be changed into the steroid hormones progesterone, testosterone, or estrogen. These molecules look quite similar, but they play very different roles in organisms. Testosterone, for example, generally masculinizes vertebrates (animals with backbones), while progesterone and estrogen play a role in regulating the ovulatory cycle.

Double X Extra: A hormone is a blood-borne signaling molecule. It can be lipid based, like testosterone, or short protein, like insulin.

Proteins

As you progress through learning biology, one thing will become more and more clear: Most cells function primarily as protein factories. It may surprise you to learn that proteins, which we often talk about in terms of food intake, are the fundamental molecule of many of life’s processes. Enzymes, for example, form a single broad category of proteins, but there are millions of them, each one governing a small step in the molecular pathways that are required for living.

Levels of Structure

Amino acids are the building blocks of proteins. A few amino acids strung together is called a peptide, while many many peptides linked together form a polypeptide. When many amino acids strung together interact with each other to form a properly folded molecule, we call that molecule a protein.

For a string of amino acids to ultimately fold up into an active protein, they must first be assembled in the correct order. The code for their assembly lies in the DNA, but once that code has been read and the amino acid chain built, we call that simple, unfolded chain the primary structure of the protein.

This chain can consist of hundreds of amino acids that interact all along the sequence. Some amino acids are hydrophobic and some are hydrophilic. In this context, like interacts best with like, so the hydrophobic amino acids will interact with one another, and the hydrophilic amino acids will interact together. As these contacts occur along the string of molecules, different conformations will arise in different parts of the chain. We call these different conformations along the amino acid chain the protein’s secondary structure.

Once those interactions have occurred, the protein can fold into its final, or tertiary structure and be ready to serve as an active participant in cellular processes. To achieve the tertiary structure, the amino acid chain’s secondary interactions must usually be ongoing, and the pH, temperature, and salt balance must be just right to facilitate the folding. This tertiary folding takes place through interactions of the secondary structures along the different parts of the amino acid chain.

The final product is a properly folded protein. If we could see it with the naked eye, it might look a lot like a wadded up string of pearls, but that “wadded up” look is misleading. Protein folding is a carefully regulated process that is determined at its core by the amino acids in the chain: their hydrophobicity and hydrophilicity and how they interact together.

In many instances, however, a complete protein consists of more than one amino acid chain, and the complete protein has two or more interacting strings of amino acids. A good example is hemoglobin in red blood cells. Its job is to grab oxygen and deliver it to the body’s tissues. A complete hemoglobin protein consists of four separate amino acid chains all properly folded into their tertiary structures and interacting as a single unit. In cases like this involving two or more interacting amino acid chains, we say that the final protein has a quaternary structure. Some proteins can consist of as many as a dozen interacting chains, behaving as a single protein unit.

A Plethora of Purposes

What does a protein do? Let us count the ways. Really, that’s almost impossible because proteins do just about everything. Some of them tag things. Some of them destroy things. Some of them protect. Some mark cells as “self.” Some serve as structural materials, while others are highways or motors. They aid in communication, they operate as signaling molecules, they transfer molecules and cut them up, they interact with each other in complex, interrelated pathways to build things up and break things down. They regulate genes and package DNA, and they regulate and package each other.

As described above, proteins are the final folded arrangement of a string of amino acids. One way we obtain these building blocks for the millions of proteins our bodies make is through our diet. You may hear about foods that are high in protein or people eating high-protein diets to build muscle. When we take in those proteins, we can break them apart and use the amino acids that make them up to build proteins of our own.

Nucleic Acids

How does a cell know which proteins to make? It has a code for building them, one that is especially guarded in a cellular vault in our cells called the nucleus. This code is deoxyribonucleic acid, or DNA. The cell makes a copy of this code and send it out to specialized structures that read it and build proteins based on what they read. As with any code, a typo–a mutation–can result in a message that doesn’t make as much sense. When the code gets changed, sometimes, the protein that the cell builds using that code will be changed, too.

Biohazard!The names associated with nucleic acids can be confusing because they all start with nucle-. It may seem obvious or easy now, but a brain freeze on a test could mix you up. You need to fix in your mind that the shorter term (10 letters, four syllables), nucleotide, refers to the smaller molecule, the three-part building block. The longer term (12 characters, including the space, and five syllables), nucleic acid, which is inherent in the names DNA and RNA, designates the big, long molecule.

DNA vs. RNA: A Matter of Structure

DNA and its nucleic acid cousin, ribonucleic acid, or RNA, are both made of the same kinds of building blocks. These building blocks are called nucleotides. Each nucleotide consists of three parts: a sugar (ribose for RNA and deoxyribose for DNA), a phosphate, and a nitrogenous base. In DNA, every nucleotide has identical sugars and phosphates, and in RNA, the sugar and phosphate are also the same for every nucleotide.

So what’s different? The nitrogenous bases. DNA has a set of four to use as its coding alphabet. These are the purines, adenine and guanine, and the pyrimidines, thymine and cytosine. The nucleotides are abbreviated by their initial letters as A, G, T, and C. From variations in the arrangement and number of these four molecules, all of the diversity of life arises. Just four different types of the nucleotide building blocks, and we have you, bacteria, wombats, and blue whales.

RNA is also basic at its core, consisting of only four different nucleotides. In fact, it uses three of the same nitrogenous bases as DNA–A, G, and C–but it substitutes a base called uracil (U) where DNA uses thymine. Uracil is a pyrimidine.

DNA vs. RNA: Function Wars

An interesting thing about the nitrogenous bases of the nucleotides is that they pair with each other, using hydrogen bonds, in a predictable way. An adenine will almost always bond with a thymine in DNA or a uracil in RNA, and cytosine and guanine will almost always bond with each other. This pairing capacity allows the cell to use a sequence of DNA and build either a new DNA sequence, using the old one as a template, or build an RNA sequence to make a copy of the DNA.

These two different uses of A-T/U and C-G base pairing serve two different purposes. DNA is copied into DNA usually when a cell is preparing to divide and needs two complete sets of DNA for the new cells. DNA is copied into RNA when the cell needs to send the code out of the vault so proteins can be built. The DNA stays safely where it belongs.

RNA is really a nucleic acid jack-of-all-trades. It not only serves as the copy of the DNA but also is the main component of the two types of cellular workers that read that copy and build proteins from it. At one point in this process, the three types of RNA come together in protein assembly to make sure the job is done right.

Anyone who watches TV, reads magazines, or flips through catalogs has seen some interesting products. Maybe they seem plausible to you, maybe they don’t. However, a little investigation shows they are based less on science and well…actually working, and more on wishful thinking. At worst they’re actual con-jobs, designed to separate you from your money as efficiently as possible (which I guess is a certain standard of success). As a result, we at Double X Science bring you “As Seen on TV!” In these features, we’ll look at some of the products shilled on talk shows and infomercials, items lurking between the articles you read in magazines, or things you might find on the shelves of the stores where you shop.

I admit it, I’m a balding dude. My forehead is gradually taking over my entire scalp, replacing my formerly thick and curly hair with a vast expanse of pink skin. Yes, dear readers: My hair was once so thick and curly that, when I wore it long and in a ponytail, ladies would ask me for my secret. (The answer: Wash it every other day with some brand of cheap shampoo and let it air dry. Don’t tell.) I don’t like the fact of my impending baldness, so I’m sympathetic toward defoliation-sufferers who want to bring their hair back at any cost.

On the other hand, I don’t think I’ll invest in any of the hair restoration products advertised in the SkyMall catalog I picked up on my flight to my brother’s wedding in San Francisco. I counted seven products in this single catalog promising to restore hair in one way or another, either reversing baldness or filling in thin patches on the scalp –- and that doesn’t include hair-coloring, extensions, or other options. I won’t cover all of them, but no fewer than three products pledge to bring hair back through the magic of lasers.

Ah, lasers. They may not have the mystique of magnets or the nous of “natural”, but they are a frequent ingredient in modern snake oil. (Come to think of it, one of the hair-restoration products may have contained snake oil. I don’t want to ask.) But while lasers can help correct nearsightedness in some cases, perform minimally invasive surgeries, and remove hair, color my scalp skeptical about their ability to restore hair.

First, a disclaimer: I’m not a biologist, a doctor, medical researcher, or in any field related to those. I’m a physicist, so the closest I ever get professionally to this topic is the “no-hair” theorem in black hole physics. The “no-hair” theorem says that black holes have very few distinguishing characteristics: only mass and rotational rate (and technically electric charge as well, though it’s hard to build up enough charge to make a difference). The analogy is that, if all humans were completely hairless, we would have a lot fewer ways to tell each other apart. In other words, this ain’t my area, so bear (bare) with me!

Night on Baldhead Mountain

Hair loss can occur for a wide variety of reasons: chemotherapy, a number of unrelated diseases, even stress. However, as humans (both men and women!) age, we all tend to lose our hair to some degree. The effect is most pronounced in male pattern baldness (a bare patch on the top of the head merging over time with the growing forehead to leave a fringe around the edges of the scalp) or female pattern baldness (a general loss of hair at the top of the scalp). However, past the age of 80, nearly everyone starts losing hair, regardless of genetics, diet, or health.

The reasons, as with so many other things, are hormonal. Hair production is governed by sex hormones: most famously testosterone, but also a less well-known cousin known as dihydrotestosterone (DHT). In some people, DHT commands the follicles — the small organs in the skin that produce and feed hair — to shrink, producing ever-finer hair until they cease operating entirely. Thus, gradual hair loss of the usual (as opposed to disease- or circumstance-derived) variety is generally preceded by the hair itself becoming thinner and fuzzier.

My naive understanding of the biology of hair loss leads me to suspect that since hormones are the culprit behind hair loss, then any hair restoration should address those hormones in some way. That alone makes me suspicious of the laser-based products SkyMall peddles. To see why, let’s look at lasers themselves.

Lasers (without sharks)

The word “laser” began as an acronym: Light Amplification by the Stimulated Emission of Radiation. The details could be an Everyday Science or Double Xplainer post in their own right, but here’s the short version. The lasers used in the SkyMall products are LED lasers, meaning they are based on the underlying physics as LED lights. An electric current kicks electrons or other electric charge carriers from one type of material to another across a junction. The excess energy the electric charge sheds during this process is given off in the form of a photon, a particle of light. Since the same amount of energy is involved every time, light from LEDs is nearly monochromatic, meaning it is almost purely one color.

The “amplification” part of the name comes by putting the LED into a special kind of cavity with reflective walls. These walls set up standing waves for the light, which interfere constructively like vibrations in a guitar string, making them brighter. However, unlike guitar strings, the production of the light in lasers is a self-feeding process, resulting in the different parts of the system synchronizing until they emit photons in concert with each other. It’s really interesting stuff, and while it’s somewhat complicated, there’s nothing really mysterious or magical about it, any more than magnets are magical.

In fact, LED lasers are so unmagical that you can buy them as cat toys. LED lasers are the inner workings of laser pointers, which you can buy very inexpensively at any number of shops.

The smell of frying follicles

One of three laser-based hair-restoration products from SkyMall. This one features built-in headphones, so you can at least listento music while you sit around looking like a fool. However,I recommend a cheaper set of headphones, since the $700price tag is a bit steep, and you’d get the same result withregards to hair restoration.

Laser hair removal uses intense lasers to selectively heat the follicles in the skin, hopefully avoiding damage to the rest of the skin. This process can slow down hair growth and cause the hair to fall out of the treated follicles, but it doesn’t always actually stop it: the treatment must be continued for a long term. Basically, the laser is damaging the follicle.

As you can imagine, that also makes me skeptical that lasers can stimulate new hair growth. Lasers produce light…and that’s it! In addition to the usual red lasers like in laser pointers, manufacturers also make infrared lasers, which are useful for surgery. While we perceive infrared as heat (which is why sunshine feels warm), I don’t think merely warming the scalp is going to make hair grow faster, or else you wouldn’t need lasers at all — an electric blanket would do just as well. Too much heating and we’re back at laser hair removal.

Similarly, visible-light lasers like the kind that seem to be in these SkyMall products simply produce red light. Because ordinary light bulbs produce a broad range of colors (white light is a mixture of all the visible-light wavelengths), sitting under a desk lamp would expose your scalp to red light. Yes, it wouldn’t be as intense as lasers, but you could do the same trick with a laser pointer from Schtaples (the Scmoffice Schmupply Schtore), provided you have the patience to hold it against your scalp for long periods of time.

The author engages in home laser hair restoration, while his catsmeow around his feet.

So, to summarize:

Hair loss in its most common forms is hormonal, so it’s unclear to me that light (whether laser or otherwise) has anything to do with it. Hair removal can be achieved with lasers, but that involves causing damage to hair follicles, not using anything intrinsic to light.

Lasers are simply very monochromatic light sources, that use synchronization of atoms on the microscopic level to do their business. There’s nothing in a laser that isn’t in ordinary light bulbs, though you can make things far more intense with a laser. However, high intensity brings us back to laser hair removal, not restoration.

As always, if a product sounds miraculous, it’s probably bunkum. If all it took to regrow hair was a glorified laser pointer, nobody would be bald! LED lasers are cheap and ubiquitous; we could all restore our hair without paying a company $700 (and listen to the music on inexpensive headphones, to boot).

Now if you’ll pardon me, I’ll get back to shining this laser pointer at my scalp.

When you read news stories about what affects a developing human in the womb or how cancer or obesity arises, you probably also see references to genes and environment. Some articles may focus on genes versus environment, or mention that something is “mostly” genetic or that the “environment” contributes to a disorder or trait in some way.What some people may not realize is that “environment” to a scientist talking about genetics may be something very different from “environment” to a non-scientist reading a news article. While a scientist may be vividly imagining a bustling microenvironment of native molecules in the way only scientists seem to do, the general reader may simply be thinking about “toxins” or “chemicals.” That’s why Double X Science is here to help with a primer on what those scientist types may mean when they talk about genes and environment. See how useful we are? Tell your friends! (Speaking of environmental influences… ).Where does environment begin and end? Let’s begin at the endNo gene is an island. Your genes consist in part of a special codethat is really an instruction manual. Your cellsrely on internal translators to decode these instructions and use them as a guide to make various proteins, the molecules that give your cells, tissues, organs, organ systems, and you much of their structure and function. Proteins do thousands of jobs, from breaking down food to building and replacing tissues (news release) to governing cell division. Most of your cells are engaged in making proteins, a complex, exquisitely regulated and multi-step process. But they don’t do it in a vacuum. That code the cell uses to build the protein? That instruction manual is susceptible to all kinds of interference. Pages get torn out or folded over or stuck together. The words of the code can be changed, sometimes subtly, sometimes unmistakably, and all kinds of factors can jumble up those words so that cell ends up making a protein that isn’t quite what was intended. It’s even possible to use the cellular version of Liquid Paper(TM) to mask the code so that the cell doesn’t recognize its existence. Sometimes, these changes have no observable effect. Sometimes, they have big bad effects, such as disease, or helpful outcomes, such as disease resistance.That code sits in a cell in a body (you) made of trillions of cells doing hundreds of different jobs, taking in things from the environment, playing host to millions of other organisms (themselves an environment), altering and shifting with every passing second as the whole system works to keep you together and functioning within certain acceptable limits for human life. All of these processes can influence the code, leading the cell to use it, change it, use only certain parts of it, Liquid Paper over it, tweak what results from its instructions, or just ignore it. It’s impossible for any code in that situation to function in the total absence of influence from its environment, in part because the code itself is just the beginning. Much of the environment’s influence is reflected in what the cell does with the instructions, not just what the instructions say. This multitude of environmental influences is one reason that even people with identical genetic codes can have differences in diseases we think of as being largely genetic. No gene–no code–is an island. You are not your genes. You are your genes and your environment.No nucleus is an island. Most of our genes are packaged neatly with the rest of our DNA around molecular spools inside a cellular vault called the nucleus. This vault is a choosy sentry, letting in only certain molecules carrying proper ID. Yet inside the nucleus, there is an environment. This environment is not “toxins” or “chemicals,” the things that many people probably think of when someone says “environment” and talks about genes. But it is a busy place with its own milieu. Some parts of the code are in use, some sit quiet, and many molecules bustle and hustle to maintain, copy, process, or protect these important instructions. Every little bit of this hustle and bustle can influence some aspect of what happens to a code in the nucleus, interfering with or enhancing its use or resulting in accidental changes that may have big effects further down the line. The nucleus is the final stop in the chain of environmental influence, wherever that influence may originate.No cell is an island. Outside of that vault is the big, wide world of the cell. The cell is the molecular version of a busy metropolis (see beautiful video, The Inner Life of the Cell, below), a complex system of cellular highways that the cell uses to deliver packages internally, take in deliveries from the outside world, and transfer the millions of molecules it’s using and making to the right places at the right time. There’s a generator, a recycling center, guards at the gate, and a protein production facility and processing plant, complete with a post office. And that cell sits in an environment, usually, of many many other cells, also busy with their duties. What happens outside of that cell affects the inside of the cell, altering traffic flows, protein production and packaging, signaling and delivery along the routes, and, ultimately, processes inside the vault called the nucleus, the final destination in the chain of environmental effects. From outside the cell, through the cell, and to the nucleus, every step along the way is one that environment can affect, all the way down to what the cell does with its genes–the codes–for the proteins it makes.

No tissue or organ is an island. A lot of cells working together to do the same thing in your body make up a tissue. Tissues combined together to perform a function are an organ. Let’s take the organ named after living, the liver. It keeps you alive by filtering your blood and reconstructing substances that might harm your cells into less-harmful compounds. Just about everything you ingest gets passed through here. When the liver takes up something like ethanol, the alcohol we ingest at wine o’ clock, and gets to work making it less awful for your body, guess what does that work? The cells that make up the liver. The liver’s environment is their environment is each individual cell’s environment, and eventually, the influence will pass to the nucleus, the final destination in the chain of environmental influence, where the code lies.You are not an island. And whatever you encounter in this world may well influence you right down to the level of your genes. But while many people might think of “toxins” or “chemicals” when they think of environmental influences on genes, your chemical exposures–and chemicals include oxygen, water, body fluids, nutrients and not-so-nutrients in your foods, medications you may take–are among many, many examples of environmental factors that may reach via a chain reaction all the way to your genes. Some of these factors affect your genes by way of your sensory system: A hug, an angry encounter, a sick child, a laugh with a friend–you respond to each of these environmental influences, often by way of hormones that have a chat with your cells. Your cells respond by adjusting how they use the code in the nucleus so that in the face of anger or love or worry, your body still functions within the essential parameters of life. Below, we list with tongue slightly in cheek a sampling of other factors that constitute an “environment” that could influence your genes and how your cell uses them and the proteins they encode. Whether you know it or not, you’re encountering a million factors every day, big and small, that may trigger some effect way down there in the nuclear vaults of your cells, one that reverberates body wide.Some examples of “environment” that might influence genesEnvironmental influence on genes and how your cells use their instructions and the resulting proteins can come from almost anywhere, any factor, from outside of you and within you. It’s not just about exposures to “bad” chemicals or “toxins.” While the list of potential environmental factors influencing genes and how the cell uses them is practically infinite, we give you just a few examples for thought below:

She gave me a few minutes to meet my daughter before she reeled me back into a state that was my new reality. “You’re not finished Jeanne. You still need to birth your placenta.” What?!?! More pushing? But I was lucky and the efforts required to bring my placenta ex vivo were minimal.

This is the second placenta my body helped make. OK,so it doesn’t EXACTLY look like meatloaf…

The idea of a placenta, which is the only human organ to completely and temporarily develop after birth, was fascinating. That thing sitting in a rectangular periwinkle bucket was what allowed me to grow another human.. inside of my body! There was no way I was not going to check it out, as well as create a permanent record of its relatively short-lived existence.

My first impression was that it looked like “meatloaf.” Not necessarily a well made meatloaf, but perhaps one that is made by my mother (sorry mom). But, alas, chaos reigned and I wasn’t able to really take a good look. However, for my second birth and hence second placenta, my midwife indulged me with a more detailed look and a mini-lesson.

Baby’s eye view: Where geekling deux spent 39 weeks and 4 days.

Her gloved hands, still wet with my blood and amniotic fluid, slid into the opening that was artificially created with a tool resembling a crocheting needle. She opened the amniotic sac wide so I could get a baby’s eye view of the crimson organ that served as a nutritional trading post between me and my new bundle of joy.

She explained that the word “placenta” comes from from the Greek word plakoeis, which translates to “flat cake” (however, I’m sure if my mom’s meatloaf was more common in ancient Greece, the placenta would be named differently). “It’s one of the defining features of being a mammal,” she explained as I was working on another mammalian trait – getting my baby to nurse for the first time.

That was about all I could mentally digest at the time, but still, more than three years later, the placenta continues to fascinate me, mostly due to the fact that it is responsible for growing new life. It’s a natural topic for this long overdue Pregnancy101post, so let’s dive in!

Development of the placenta

It all starts when a fertilized egg implants itself into the wall of the uterus. But, in order to fully understand how it works, we should start with an overview of the newly formed embryo.

The very early stages of us (and many other things that are alive).

The trophoblast invades the uterus,leading to implantation of the blastocyst.

As soon as a male sperm cell fuses with a female egg cell, fertilization occurs and the cells begin to multiply. But, they remain contained within a tiny sphere. As the cells continue to divide, they are given precise instructions depending on their location within that sphere, and begin to transform into specific cell types. This process, which is called cellular differentiation, actually seals the fate every cell in our body, sort of like how we all have different jobs – some of us are transport things, some of us are involved in policing the neighborhoods, some of us build structures, some of us communicate information, some of us deal with food, some of us get rid of waste, etc. Every cell gets a job (it’s the only example of 100% employment rates!).

Now back to the cells in the fertilized egg. As they start to learn what their specific job will be, the cells within the sphere will start to organize themselves. After about 5 days after fertilization, the sphere of cells becomes something called a blastocyst, which readies itself for implantationinto the wall of the uterus.

The act of implantation is largely due to the cells found on the perimeter of the blastocyst sphere. These cells, collectively known as the trophoblast, release a very important hormone – human chorionic gonadotropin (hCG) – that tells the uterus to prepare for it’s new tenant. (If you recall, hCG is the hormone picked up by pregnancy tests.) Around day 7, the trophoblast cells start to invade the lining of the uterus, and begin to form the placenta. It is at this point that pregnancy officially begins. (Here is a cool video, created by the UNSW Embryology Department, showing the process of implantation.)

Structure of the placenta

Eventually the trophoblast becomes the recognizable organ that is the placenta. Consider the “flat cake” analogy, with the top of the cake being the fetal side (the side that is in contact with the baby), and the bottom of the cake being the maternal side (the side that is in contact with the mother).

Cross section of the placenta: Blood vessels originating from the fetus sit in a pool of maternal blood, which is constantly replenished my maternal arteries and veins. The red represents oxygenated blood, and the blue represents de-oxygenated blood.

Projecting from the center of the fetal side of the placenta are two arteries and one vein, coiled together in a long, rubbery rope, often bluish-grey in color. This umbilical cord serves as the tunnel through which nutrients and waste are shuttled, and essentially serves to plug the baby into the mother’s metabolic processes. At the umbilical cord-placenta nexus, the umbilical cord arteries and vein branch out into a network of blood vessels, which further divide into a tree-like mass of vessels within the placenta.

These tree-like masses originating from the umbilical cord (and thus fetus) sit in a cavity called the intervillous space, and are bathed in nutrient-rich maternal blood. This maternal blood, which provides the fetus with a means for both nutrient delivery and waste elimination, is continually replenished via a network of maternal arteries and veins that feed into the intervillous space. Furthermore, these arteries and veins help to anchor the placenta into the uterine wall. One of the most interesting aspects about the mother-feus relationship is that the blood vessel connection is indirect. This helps to prevent a detrimental immune response, which could lead to immunological rejection of the fetus (sort of like how a transplanted organ can become rejected by the recipient).

Functions of the placenta

Just like a plant needs sunlight, oxygen, and water to grow, a baby needs all sorts of nutrients to develop. And since a baby also produces waste, by nature of it being alive and all, there is an absolute requirement for waste removal. However, because we can’t just give a developing fetus food or a bottle, nor are we able to change diapers in utero, the onus lies completely on the biological mother.

This is where the placenta comes in. Because the fetus is plugged into the circulatory system of the mother via the umbilical cord and placenta, the fetus is provided with necessary nutrients and a mechanism to get rid of all the byproducts of metabolism. Essentially, the placenta acts as a waitress of sorts – providing the food, and cleaning it all up when the fetus is done eating.

But it’s not just about nutrition and waste. The placenta also serves as a hormone factory, making and secreting biological chemicals to help sustain the pregnancy. I mentioned above that the placenta produces hCG, which pretty much serves as a master regulator for pregnancy in that it helps control the production of maternally produced hormones, estrogen and progesterone. It also helps to suppress the mother’s immunological response to the placenta (along with other factors), which cloaks the growing baby, thereby hiding it from being viewed as a “foreign” invader (like a virus or bacteria).

Another hormone produced by the placenta is human placental lactogen (hPL), which tells the mother to increase her mammary tissue. This helps mom prepare for nursing her baby once it’s born, and is the primary reason why our boobs tend to get bigger when we are pregnant. (Yay for big boobies, but my question is, what the hell transforms our rear ends into giant double cheeseburgers, and what biological purpose does that serve?? But I digress…)

Despite the fact that the mother’s circulatory system remains separate from the baby’s circulatory system, there are a clear mixing of metabolic products (nutrients, waste, hormones, etc). In essence, if it is in mom’s blood stream, it will very likely pass into baby’s blood stream. This is the very reason that pregnant mothers are strongly advised to stay away from cigarettes, drugs, alcohol, and other toxic chemicals, all of which can easily pass through the placental barrier lying between mother and fetus. When moms do not heed this warning, the consequences can be devastating to the developing fetus, potentially leading to birth defects or even miscarriage.

There are also situations that could compromise the functions of the placenta – restriction of blood supply, loss of placental tissue, muted placental growth, just to name a few – reducing the chances of getting and/or staying pregnant. This placental insufficiency is generally accompanied by slow growth of the uterus, low rate of weight gain, and most importantly, reduced fetal growth.

And it’s not just the growth of the placenta that is important – where the placenta attaches to the uterus is also very important. When the placenta grows on top of the opening of the birth canal, the chances for a normal, vaginal birth are obliterated. This condition, known as placenta previa, is actually quite dangerous and can cuase severe bleeding in the third trimester. 0.5% of all women experience this, and it is one of the true medical conditions that absolutely requires a C-section.

Then, there is the issue of attachment. If the placenta doesn’t attach well to the uterus, it could end up peeling away from the uterine wall, which can cause vaginal bleeding, as well as deprive the baby from nutrient delivery and waste disposal. This abruption of the placenta is complicated by the use of drugs, smoking, blood clotting disorders, high blood pressure, or if the mother has diabetes or a history of placental abruption.

Conversely, there are times when the blood vessels originating from the placenta implant too deeply into the uterus, which can lead to a placenta accreta. If this occurs, the mother generally delivers via C-section, followed by a complete hysterectomy.

Cultural norms and the placenta

There are many instances where the placenta plays a huge role in the culture of a society. For instance, both the Maori people of New Zealand and the Navajopeople of Southwestern US will bury the placenta. There is also some folklore associated with the placenta, and several societies believe that it is alive, pehaps serving as a friend for the baby. But the tradition that seems to be making it’s way into the granola culture of the US is one that can be traced back to traditional Chinese practices: eating the placenta.

Placentophagy, or eating one’s own placenta, is very common among a variety of mammalian species. Biologically speaking, it is thought that animals that eat their own placenta do so to hide fresh births from predators, thereby increasing the chances of their babies’ survival. Others have suggested that eating the nutrient-rich placenta helps mothers to recover after giving birth.

However, these days, a growing number of new mothers are opting to ingest that which left their own body (likely) through their own vaginas. And they are doing so though a very expensive process involving dehydrating and encapsulating placental tissue.

Why would one go through this process? The claims are that placentophagy will help ward of post partum depression, increase the supply of milk in a lactating mother, and even slow down the ageing process. But, alas, these are some pretty bold claims that are substantiated only by anecdata, and not actual science (see this).

So, even though my placentas looked like meatloaf, there was no way I was eating them. If you are considering this, I’d approach the issue with great skepticism. There are many a people who will take advantage of maternal vulnerabilities in the name of cold hard cash. And, always remember, if the claims sound to good to be true, they probably are!

Thanks for tuning into this issue of Pregnancy101, and enjoy this hat, and a video!